5lnc | pdb_00005lnc

Structure of SPX domain of the yeast inorganic polyphophate polymerase Vtc4 crystallized by carrier-driven crystallization in fusion with the macro domain of human histone macroH2A1.1

spinqualitylabelsall models 5lnc, resolution 3.29Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lnc is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 5iit Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VTC4_YEAST] Component of the vacuolar transporter chaperone (VTC) complex, which plays a role in vacuolar membrane fusion. Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation. Publication Abstract from PubMed Obtaining well-ordered crystals remains a significant challenge in protein X-ray crystallography. Carrier-driven crystallization can facilitate crystal formation and structure solution of difficult target proteins. We obtained crystals of the small and highly flexible SPX domain from the yeast vacuolar transporter chaperone 4 (Vtc4) when fused to a C-terminal, non-cleavable macro tag derived from human histone macroH2A1.1. Initial crystals diffracted to 3.3 A resolution. Reductive protein methylation of the fusion protein yielded a new crystal form diffracting to 2.1 A. The structures were solved by molecular replacement, using isolated macro domain structures as search models. Our findings suggest that macro domain tags can be employed in recombinant protein expression in E. coli, and in carrier-driven crystallization. The macro domain as fusion tag for carrier-driven crystallization.,Wild R, Hothorn M Protein Sci. 2016 Oct 24. doi: 10.1002/pro.3073. PMID:27774698 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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